SitesBLAST
Comparing PP_3726 PP_3726 Enoyl-CoA hydratase/isomerase family protein to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
41% identity, 97% coverage: 8:264/264 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A67), F69 (≠ W72), L80 (= L81), N84 (≠ G85), A108 (≠ G115), S111 (≠ D118), A130 (≠ G137), F131 (≠ Y138), L136 (≠ Y143), P138 (= P145), D139 (= D146), A224 (≠ E231), G234 (= G241)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (= R61), A62 (= A65), Q64 (≠ A67), D65 (= D68), L66 (= L69), Y76 (≠ A77), A108 (≠ G115), F131 (≠ Y138), D139 (= D146)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
41% identity, 97% coverage: 8:264/264 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A67), L68 (= L81), N72 (≠ G85), A96 (≠ G115), S99 (≠ D118), A118 (≠ G137), F119 (≠ Y138), L124 (≠ Y143), P126 (= P145), N127 (≠ D146), A212 (≠ E231), G222 (= G241)
- binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ R27), A59 (= A65), Q61 (≠ A67), D62 (= D68), L63 (= L69), L68 (= L81), Y71 (= Y84), A94 (≠ V113), G95 (= G114), A96 (≠ G115), F119 (≠ Y138), I122 (≠ M141), L124 (≠ Y143), N127 (≠ D146), F234 (≠ S253), K237 (≠ R256)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 98% coverage: 7:264/264 of query aligns to 5:259/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ W72), S82 (≠ T87), R86 (≠ H91), G110 (= G115), E113 (≠ D118), P132 (≠ G137), E133 (≠ Y138), I138 (≠ Y143), P140 (= P145), G141 (≠ D146), A226 (≠ E231), F236 (≠ G241)
- binding coenzyme a: K24 (≠ Q26), L25 (≠ R27), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (≠ L69), P132 (≠ G137), R166 (≠ E170), F248 (≠ S253), K251 (≠ R256)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
36% identity, 94% coverage: 15:261/264 of query aligns to 24:268/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 94% coverage: 16:264/264 of query aligns to 17:260/260 of 2hw5C
- active site: A68 (= A67), M73 (≠ L81), S83 (≠ H91), L87 (= L95), G111 (= G115), E114 (≠ D118), P133 (≠ G137), E134 (≠ Y138), T139 (≠ Y143), P141 (= P145), G142 (≠ D146), K227 (≠ E231), F237 (≠ G241)
- binding crotonyl coenzyme a: K26 (≠ E25), A27 (≠ Q26), L28 (≠ R27), A30 (= A29), K62 (≠ R61), I70 (≠ L69), F109 (≠ V113)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 7:262/264 of query aligns to 4:250/250 of 3q0gD
- active site: A64 (= A67), M69 (vs. gap), T75 (≠ A77), F79 (≠ L81), G103 (= G115), E106 (≠ D118), P125 (≠ G137), E126 (≠ Y138), V131 (≠ Y143), P133 (= P145), G134 (≠ D146), L219 (≠ E231), F229 (≠ G241)
- binding Butyryl Coenzyme A: F225 (≠ G237), F241 (≠ S253)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 97% coverage: 7:262/264 of query aligns to 5:255/255 of 3q0jC
- active site: A65 (= A67), M70 (≠ W72), T80 (= T87), F84 (≠ H91), G108 (= G115), E111 (≠ D118), P130 (≠ G137), E131 (≠ Y138), V136 (≠ Y143), P138 (= P145), G139 (≠ D146), L224 (≠ E231), F234 (≠ G241)
- binding acetoacetyl-coenzyme a: Q23 (≠ E25), A24 (≠ Q26), L25 (≠ R27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (≠ L69), K68 (≠ A70), M70 (≠ W72), F84 (≠ H91), G107 (= G114), G108 (= G115), E111 (≠ D118), P130 (≠ G137), E131 (≠ Y138), P138 (= P145), G139 (≠ D146), M140 (≠ A147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 97% coverage: 7:262/264 of query aligns to 5:255/255 of 3q0gC
- active site: A65 (= A67), M70 (≠ W72), T80 (= T87), F84 (≠ H91), G108 (= G115), E111 (≠ D118), P130 (≠ G137), E131 (≠ Y138), V136 (≠ Y143), P138 (= P145), G139 (≠ D146), L224 (≠ E231), F234 (≠ G241)
- binding coenzyme a: L25 (≠ R27), A63 (= A65), I67 (≠ L69), K68 (≠ A70), Y104 (≠ T111), P130 (≠ G137), E131 (≠ Y138), L134 (≠ M141)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 97% coverage: 7:262/264 of query aligns to 4:254/256 of 3h81A
- active site: A64 (= A67), M69 (≠ W72), T79 (= T87), F83 (≠ H91), G107 (= G115), E110 (≠ D118), P129 (≠ G137), E130 (≠ Y138), V135 (≠ Y143), P137 (= P145), G138 (≠ D146), L223 (≠ E231), F233 (≠ G241)
- binding calcium ion: F233 (≠ G241), Q238 (≠ G246)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 93% coverage: 16:261/264 of query aligns to 17:257/260 of 1dubA
- active site: A68 (= A67), M73 (≠ L81), S83 (≠ H91), L87 (= L95), G111 (= G115), E114 (≠ D118), P133 (≠ G137), E134 (≠ Y138), T139 (≠ Y143), P141 (= P145), G142 (≠ D146), K227 (≠ E231), F237 (≠ G241)
- binding acetoacetyl-coenzyme a: K26 (≠ E25), A27 (≠ Q26), L28 (≠ R27), A30 (= A29), A66 (= A65), A68 (= A67), D69 (= D68), I70 (≠ L69), Y107 (≠ T111), G110 (= G114), G111 (= G115), E114 (≠ D118), P133 (≠ G137), E134 (≠ Y138), L137 (≠ M141), G142 (≠ D146), F233 (≠ G237), F249 (≠ S253)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 93% coverage: 16:261/264 of query aligns to 15:255/258 of 1ey3A
- active site: A66 (= A67), M71 (≠ L81), S81 (≠ H91), L85 (= L95), G109 (= G115), E112 (≠ D118), P131 (≠ G137), E132 (≠ Y138), T137 (≠ Y143), P139 (= P145), G140 (≠ D146), K225 (≠ E231), F235 (≠ G241)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E25), L26 (≠ R27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (≠ L69), L85 (= L95), W88 (vs. gap), G109 (= G115), P131 (≠ G137), L135 (≠ M141), G140 (≠ D146)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
31% identity, 94% coverage: 14:261/264 of query aligns to 45:287/290 of P14604
- E144 (≠ D118) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ Y138) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 93% coverage: 16:261/264 of query aligns to 17:255/258 of 1mj3A
- active site: A68 (= A67), M73 (≠ L81), S83 (≠ H91), L85 (= L93), G109 (= G115), E112 (≠ D118), P131 (≠ G137), E132 (≠ Y138), T137 (≠ Y143), P139 (= P145), G140 (≠ D146), K225 (≠ E231), F235 (≠ G241)
- binding hexanoyl-coenzyme a: K26 (≠ E25), A27 (≠ Q26), L28 (≠ R27), A30 (= A29), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (≠ L69), G109 (= G115), P131 (≠ G137), E132 (≠ Y138), L135 (≠ M141), G140 (≠ D146)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 93% coverage: 16:261/264 of query aligns to 16:251/254 of 2dubA
- active site: A67 (= A67), M72 (≠ L81), S82 (≠ A92), G105 (= G115), E108 (≠ D118), P127 (≠ G137), E128 (≠ Y138), T133 (≠ Y143), P135 (= P145), G136 (≠ D146), K221 (≠ E231), F231 (≠ G241)
- binding octanoyl-coenzyme a: K25 (≠ E25), A26 (≠ Q26), L27 (≠ R27), A29 (= A29), A65 (= A65), A67 (= A67), D68 (= D68), I69 (≠ L69), K70 (≠ A70), G105 (= G115), E108 (≠ D118), P127 (≠ G137), E128 (≠ Y138), G136 (≠ D146), A137 (= A147)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
32% identity, 84% coverage: 11:233/264 of query aligns to 8:232/269 of 1nzyB
- active site: C61 (= C64), F64 (≠ A67), I69 (≠ W72), A86 (vs. gap), H90 (≠ T87), G114 (= G115), G117 (≠ D118), A136 (≠ G137), W137 (≠ Y138), I142 (≠ Y143), N144 (≠ P145), D145 (= D146), E230 (= E231)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E25), H23 (≠ Q26), R24 (= R27), A62 (= A65), F64 (≠ A67), Y65 (≠ D68), L66 (= L69), R67 (≠ A70), W89 (= W86), G113 (= G114), G114 (= G115), A136 (≠ G137), W137 (≠ Y138), D145 (= D146), T146 (≠ A147)
- binding calcium ion: G49 (≠ R52), L202 (= L203), A203 (= A204), A205 (≠ G206), T207 (= T208), Q210 (≠ Y211)
- binding phosphate ion: E57 (≠ G60), N108 (= N109), K188 (≠ D189), R192 (≠ P193)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 93% coverage: 20:264/264 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ W72), L84 (vs. gap), R88 (≠ T87), G112 (= G115), E115 (≠ D118), T134 (≠ G137), E135 (≠ Y138), I140 (≠ Y143), P142 (= P145), G143 (≠ D146), A228 (≠ Q229), L238 (= L239)
- binding coenzyme a: S24 (≠ E25), R25 (≠ Q26), R26 (= R27), A28 (= A29), A65 (= A65), D68 (= D68), L69 (= L69), K70 (≠ A70), L110 (≠ V113), G111 (= G114), T134 (≠ G137), E135 (≠ Y138), L138 (≠ M141), R168 (≠ L171)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
31% identity, 84% coverage: 11:233/264 of query aligns to 8:232/269 of 1jxzB
- active site: C61 (= C64), F64 (≠ A67), I69 (≠ W72), A86 (vs. gap), Q90 (≠ T87), G113 (= G114), G114 (= G115), G117 (≠ D118), A136 (≠ G137), W137 (≠ Y138), I142 (≠ Y143), N144 (≠ P145), D145 (= D146), E230 (= E231)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E25), H23 (≠ Q26), R24 (= R27), A62 (= A65), F64 (≠ A67), Y65 (≠ D68), L66 (= L69), R67 (≠ A70), W89 (= W86), G113 (= G114), A136 (≠ G137), W137 (≠ Y138), I142 (≠ Y143), D145 (= D146), T146 (≠ A147)
- binding calcium ion: G49 (≠ R52), L202 (= L203), A203 (= A204), A205 (≠ G206), T207 (= T208), Q210 (≠ Y211)
Sites not aligning to the query:
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 84% coverage: 6:226/264 of query aligns to 9:235/378 of Q9LKJ1
- G70 (≠ A67) mutation to S: Loss of activity.
- E142 (≠ Y138) mutation to A: Loss of activity.
- D150 (= D146) mutation to G: Reduced activity.
A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
31% identity, 84% coverage: 11:233/264 of query aligns to 8:232/269 of A5JTM5
- R24 (= R27) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ Q37) mutation to T: Forms inclusion bodies.
- E43 (≠ A46) mutation to A: No effect on catalytic activity.
- D45 (= D48) mutation to A: No effect on catalytic activity.
- D46 (≠ P49) mutation to A: No effect on catalytic activity.
- G63 (= G66) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ A67) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
- Y65 (≠ D68) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ A70) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E71) mutation to T: No effect on catalytic activity.
- H81 (≠ S83) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ Y84) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (= W86) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ T87) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
- H94 (= H91) mutation to Q: No effect on catalytic activity.
- A112 (≠ V113) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
- G113 (= G114) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
- G114 (= G115) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G116) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D124) mutation to T: No effect on catalytic activity.
- D129 (≠ A130) mutation to T: No effect on catalytic activity.
- W137 (≠ Y138) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D146) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ R164) mutation to T: No effect on catalytic activity.
- E175 (≠ R176) mutation to D: No effect on catalytic activity.
- W179 (≠ A180) mutation to F: No effect on catalytic activity.
- H208 (≠ F209) mutation to Q: No effect on catalytic activity.
- R216 (≠ L217) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E233) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
Sites not aligning to the query:
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
39% identity, 75% coverage: 8:205/264 of query aligns to 3:186/224 of 3p85A
- active site: L62 (≠ A67), L67 (≠ W72), P68 (≠ A73), G92 (= G115), E95 (≠ D118), T114 (≠ G137), H115 (≠ Y138), L120 (≠ Y143), P122 (= P145), T123 (≠ D146)
- binding calcium ion: D43 (= D47), D45 (≠ P49)
Sites not aligning to the query:
Query Sequence
>PP_3726 PP_3726 Enoyl-CoA hydratase/isomerase family protein
MTTPSSSLLSKVEAGVAWITLNRPEQRNALDIPTLKQLHALLDSHADDPAVRVVVLTGSG
RSFCAGADLAEWAAAEAAGTLESYGWTETAHALMLRLHSLDKPTIAAINGTAVGGGMDLS
LCCDLRIAAASARFKAGYTSMGYSPDAGASWHLPRLIGSEQAKRLLFLDELWGADRALAA
GLVSEVCADEQLPAVAAELAGRLANGPTFAYAQTKRLIRDGARRTLAEQLEAERHAGLLC
GRSQDGAEALQASVERRTPRFTGQ
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory